The JI
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     
 

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Berkower, I.
Right arrow Articles by Berzofsky, J. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Berkower, I.
Right arrow Articles by Berzofsky, J. A.

The Journal of Immunology, Vol 136, Issue 7 2498-2503, Copyright © 1986 by American Association of Immunologists

ARTICLES

Molecular mapping of a histocompatibility-restricted immunodominant T cell epitope with synthetic and natural peptides: implications for T cell antigenic structure

I Berkower, GK Buckenmeyer and JA Berzofsky

We have prepared synthetic and natural peptides that have allowed delineation of a major antigenic site of myoglobin recognized by histocompatibility (I-Ed)-restricted T cell clones. The smallest peptide capable of stimulating T cell proliferation consisted of residues 136-146. Residues Glu 136, Lys 140, and Lys 145 were essential for antigenicity, whereas Lys 133 and Tyr 146 added potency but were not required for antigenicity. The periodicity of these residues suggests that folding the peptide into its native alpha-helical structure may be essential for antigenicity either by forming a hydrophilic binding site for the T cell receptor or by participating in antigen presentation. The same folding could also produce a hydrophobic site on the opposite side of the alpha-helix that could participate in hydrophobic interactions. The extrapolation of these findings to other known peptide antigens suggests that this tendency to form an amphipathic alpha-helix may be a general property of antigenic sites recognized by T cells, perhaps due to a different functional role of each type of site in eliciting T cell responses.


This article has been cited by other articles:


Home page
 J. Virol.Home page
K. Yusim, C. Kesmir, B. Gaschen, M. M. Addo, M. Altfeld, S. Brunak, A. Chigaev, V. Detours, and B. T. Korber
Clustering Patterns of Cytotoxic T-Lymphocyte Epitopes in Human Immunodeficiency Virus Type 1 (HIV-1) Proteins Reveal Imprints of Immune Evasion on HIV-1 Global Variation
J. Virol., July 29, 2002; 76(17): 8757 - 8768.
[Abstract] [Full Text] [PDF]

Home page
 ScienceHome page
S Roy, M. Scherer, T. Briner, J. Smith, and M. Gefter
Murine MHC polymorphism and T cell specificities
Science, May 5, 1989; 244(4904): 572 - 575.
[Abstract] [PDF]

Home page
 ScienceHome page
S Buus, A Sette, S. Colon, C Miles, and H. Grey
The relation between major histocompatibility complex (MHC) restriction and the capacity of Ia to bind immunogenic peptides
Science, March 13, 1987; 235(4794): 1353 - 1358.
[Abstract] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Website Copyright © 1986 by The American Association of Immunologists, Inc. All rights reserved.
All Contents Copyright © 1986 by The American Association of Immunologists, Inc. All rights reserved.